Targeting Bacterial Membranes: Identification of Pseudomonas aeruginosa D-Arabinose-5P Isomerase and NMR Characterisation of its Substrate Recognition and Binding Properties.
Targeting Bacterial Membranes: Identification of Pseudomonas aeruginosa D-Arabinose-5P Isomerase and NMR Characterisation of its Substrate Recognition and Binding Properties.
Targeting Bacterial Membranes: Identification of Pseudomonas aeruginosa D-Arabinose-5P Isomerase and NMR Characterisation of its Substrate Recognition and Binding Properties.
Chembiochem. 2011 Feb 17;
Authors: Airoldi C, Sommaruga S, Merlo S, Sperandeo P, Cipolla L, Polissi A, Nicotra F
The identification and characterisation of Pseudomonas aeruginosa KdsD (Pa-KdsD), a D-arabinose-5P isomerase involved in the biosynthesis of 3-deoxy-D-manno-oct-2-ulosonic acid and thus of lipopolysaccharide (LPS), are reported. We have demonstrated that KdsD is essential for P. aeruginosa survival and thus represents a key target for the development of novel antibacterial drugs. The key amino acid residues for protein activity have been identified. The structural requirements for substrate recognition and binding have been characterised for the wild-type protein, and the effect of mutations of the key residues on catalytic activity and binding have been evaluated by saturation transfer difference (STD) NMR spectroscopy. Our data provide important structural information for the rational design of new KdsD inhibitors as potential antibacterial drugs.
PMID: 21337483 [PubMed - as supplied by publisher]
Transient Enzyme–Substrate Recognition Monitored by Real-Time NMR
Transient Enzyme–Substrate Recognition Monitored by Real-Time NMR
Caroline Haupt, Rica Patzschke, Ulrich Weininger, Stefan Gro?ger, Michael Kovermann and Jochen Balbach
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja2010048/aop/images/medium/ja-2011-010048_0002.gif
Journal of the American Chemical Society
DOI: 10.1021/ja2010048
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/nknzYbs0FNE
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Transient enzyme-substrate recognition monitored by real-time NMR.
Transient enzyme-substrate recognition monitored by real-time NMR.
Transient enzyme-substrate recognition monitored by real-time NMR.
J Am Chem Soc. 2011 Jun 10;
Authors: Haupt C, Patzschke R, Weininger U, Gröger S, Kovermann M, Balbach J
Slow protein folding processes during which kinetic folding intermediates occur for an extended time can lead to aggregation and dysfunction in living cells. Therefore protein folding helpers have evolved, which prevent proteins from aggregation and/ or speed up folding processes. In this study we present the...
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Metabolic relationship between polyhydroxyalkanoic acid and rhamnolipid synthesis in Pseudomonas aeruginosa: comparative ¹³C NMR analysis of the products in wild-type and mutants.
Metabolic relationship between polyhydroxyalkanoic acid and rhamnolipid synthesis in Pseudomonas aeruginosa: comparative ¹³C NMR analysis of the products in wild-type and mutants.
Metabolic relationship between polyhydroxyalkanoic acid and rhamnolipid synthesis in Pseudomonas aeruginosa: comparative ¹³C NMR analysis of the products in wild-type and mutants.
J Biotechnol. 2011 Jan 10;151(1):30-42
Authors: Choi MH, Xu J, Gutierrez M, Yoo T, Cho YH, Yoon SC
Polyhydroxyalkanoic acids (PHAs) and rhamnolipids considered as biotechnologically important...
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[NMR paper] Substrate recognition by the Lyn protein-tyrosine kinase. NMR structure of the immuno
Substrate recognition by the Lyn protein-tyrosine kinase. NMR structure of the immunoreceptor tyrosine-based activation motif signaling region of the B cell antigen receptor.
Related Articles Substrate recognition by the Lyn protein-tyrosine kinase. NMR structure of the immunoreceptor tyrosine-based activation motif signaling region of the B cell antigen receptor.
J Biol Chem. 2000 May 26;275(21):16174-82
Authors: Gaul BS, Harrison ML, Geahlen RL, Burton RA, Post CB
The immunoreceptor tyrosine-based activation motif (ITAM) plays a central role...
[NMR paper] Solution structure of Fe(II) cytochrome c551 from Pseudomonas aeruginosa as determine
Solution structure of Fe(II) cytochrome c551 from Pseudomonas aeruginosa as determined by two-dimensional 1H NMR.
Related Articles Solution structure of Fe(II) cytochrome c551 from Pseudomonas aeruginosa as determined by two-dimensional 1H NMR.
Biochemistry. 1991 Sep 17;30(37):9040-6
Authors: Detlefsen DJ, Thanabal V, Pecoraro VL, Wagner G
The solution structure of Fe(II) cytochrome c551 from Pseudomonas aeruginosa based on 2D 1H NMR data is reported. Two sets of structure calculations were completed with a combination of simulated annealing...
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[NMR paper] Solution structure of Fe(II) cytochrome c551 from Pseudomonas aeruginosa as determine
Solution structure of Fe(II) cytochrome c551 from Pseudomonas aeruginosa as determined by two-dimensional 1H NMR.
Related Articles Solution structure of Fe(II) cytochrome c551 from Pseudomonas aeruginosa as determined by two-dimensional 1H NMR.
Biochemistry. 1991 Sep 17;30(37):9040-6
Authors: Detlefsen DJ, Thanabal V, Pecoraro VL, Wagner G
The solution structure of Fe(II) cytochrome c551 from Pseudomonas aeruginosa based on 2D 1H NMR data is reported. Two sets of structure calculations were completed with a combination of simulated annealing...
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[NMR paper] The detection of proline isomerase activity in FK506-binding protein by two-dimension
The detection of proline isomerase activity in FK506-binding protein by two-dimensional 1H NMR exchange spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles The detection of proline isomerase activity in FK506-binding protein by two-dimensional 1H NMR exchange spectroscopy.
Biochem Biophys Res Commun. 1990 Aug 31;171(1):445-50
Authors: Justice RM, Kline AD, Sluka JP, Roeder WD, Rodgers GH, Roehm N, Mynderse JS
1H NMR assignments of the trans and cis isomers of...